<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Domenech, Jordi</style></author><author><style face="normal" font="default" size="100%">Orihuela, Ruben</style></author><author><style face="normal" font="default" size="100%">Mir, Gisela</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author><author><style face="normal" font="default" size="100%">Atrian, Silvia</style></author><author><style face="normal" font="default" size="100%">Capdevila, Merce</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Cd(II)-binding abilities of recombinant Quercus suber metallothionein: bridging the gap between phytochelatins and metallothioneins.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cadmium</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium–His binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutathione</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolic Detoxication</style></keyword><keyword><style  face="normal" font="default" size="100%">metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Metallothionein: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Phytochelatins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant Proteins: metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sulfide ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast complementation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007///</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/17503092</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">867 - 882</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this work, we have analyzed both at stoichiometric and at conformational level the Cd(II)-binding features of a type 2 plant metallothionein (MT) (the cork oak, Quercus suber, QsMT). To this end four peptides, the wild-type QsMT and three constructs previously engineered to characterize its Zn(II)- and Cu(I)-binding behaviour, were heterologously produced in Escherichia coli cultures supplemented with Cd(II), and the corresponding complexes were purified up to homogeneity. The Cd(II)-binding ability of these recombinant peptides was determined through the chemical, spectroscopic and spectrometric characterization of the recovered clusters. Recombinant synthesis of the four QsMT peptides in cadmium-rich media rendered complexes with a higher metal content than those obtained from zinc-supplemented cultures and, consequently, the recovered Cd(II) species are nonisostructural to those of Zn(II). Also of interest is the fact that three out of the four peptides yielded recombinant preparations that included S(2-)-containing Cd(II) complexes as major species. Subsequently, the in vitro Zn(II)/Cd(II) replacement reactions were studied, as well as the in vitro acid denaturation and S(2-) renaturation reactions. Finally, the capacity of the four peptides for preventing cadmium deleterious effects in yeast cells was tested through complementation assays. Consideration of all the results enables us to suggest a hairpin folding model for this typical type 2 plant Cd(II)-MT complex, as well as a nonnegligible role of the spacer in the detoxification function of QsMT towards cadmium.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><notes><style face="normal" font="default" size="100%">The following values have no corresponding Zotero field:&lt;br/&gt;accession-num: 17503092</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors></contributors><titles><title><style face="normal" font="default" size="100%">The Cd(II)-binding abilities of recombinant Quercus suber metallothionein: bridging the gap between phytochelatins and metallothioneins.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">867-882</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this work, we have analyzed both at stoichiometric and at conformational level the Cd(II)-binding features of a type 2 plant metallothionein (MT) (the cork oak, Quercus suber, QsMT). To this end four peptides, the wild-type QsMT and three constructs previously engineered to characterize its Zn(II)- and Cu(I)-binding behaviour, were heterologously produced in Escherichia coli cultures supplemented with Cd(II), and the corresponding complexes were purified up to homogeneity. The Cd(II)-binding ability of these recombinant peptides was determined through the chemical, spectroscopic and spectrometric characterization of the recovered clusters. Recombinant synthesis of the four QsMT peptides in cadmium-rich media rendered complexes with a higher metal content than those obtained from zinc-supplemented cultures and, consequently, the recovered Cd(II) species are nonisostructural to those of Zn(II). Also of interest is the fact that three out of the four peptides yielded recombinant preparations that included S(2-)-containing Cd(II) complexes as major species. Subsequently, the in vitro Zn(II)/Cd(II) replacement reactions were studied, as well as the in vitro acid denaturation and S(2-) renaturation reactions. Finally, the capacity of the four peptides for preventing cadmium deleterious effects in yeast cells was tested through complementation assays. Consideration of all the results enables us to suggest a hairpin folding model for this typical type 2 plant Cd(II)-MT complex, as well as a nonnegligible role of the spacer in the detoxification function of QsMT towards cadmium.</style></abstract><accession-num><style face="normal" font="default" size="100%">17503092</style></accession-num></record></records></xml>